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GeneE
10 sources retrieved Β· Most recent: April 2026 Β· Index updated 14 days ago
β“˜GeneE is for informational purposes only. It is not a substitute for professional medical advice, diagnosis, or treatment.
LIAS
lipoic acid synthetase
Chromosome 4 Β· 4p14
NCBI Gene: 11019Ensembl: ENSG00000121897.15HGNC: HGNC:16429UniProt: A0A1X7SBR7
26PubMed Papers
21Diseases
0Drugs
32Pathogenic Variants
CLINICAL
OMIM Disease Gene
DATA QUALITY
βœ“ Experimental GO Evidenceβœ“ Swiss-Prot Reviewed
mitochondrionlipoate synthase activityresponse to lipopolysaccharidelipoate biosynthetic processlipoic acid synthetase deficiencygenetic disorderneurodegenerative diseasemitochondrial disease
✦AI Summary

LIAS (lipoic acid synthetase) is a mitochondrial enzyme that catalyzes the biosynthesis of lipoic acid, a critical cofactor for mitochondrial metabolism. The enzyme performs radical-mediated insertion of sulfur atoms to convert octanoylated protein domains into lipoylated derivatives on key mitochondrial enzymes involved in the TCA cycle 1. LIAS functions through direct interaction with ferredoxin 1 (FDX1), which serves as an essential electron donor and regulatory partner. This FDX1-LIAS interaction promotes functional binding to lipoyl carrier proteins like GCSH, enabling cellular protein lipoylation that is crucial for maintaining mitochondrial respiration and cell viability under metabolic stress conditions 1. Beyond its metabolic role, LIAS has emerged as a key regulator of cuproptosis, a copper-dependent form of cell death. In this pathway, LIAS works alongside FDX1 to mediate copper-induced cytotoxicity, with dysregulation of both proteins observed in various pathological conditions 23. Clinically, LIAS dysfunction is associated with severe metabolic disorders characterized by hyperglycinemia, lactic acidosis, and seizures. The protein's dual role in essential metabolism and regulated cell death makes it a potential therapeutic target in cancer, cardiovascular disease, and neurodegeneration 45.

Sources cited
1
LIAS directly interacts with FDX1 to regulate cellular protein lipoylation and maintain mitochondrial function
PMID: 37453661
2
LIAS is upregulated in radiation-resistant tumors and serves as a key regulator of cuproptosis
PMID: 39300223
3
LIAS levels decrease during triptolide-induced cuproptosis in cervical cancer cells
PMID: 39198750
4
PCSK9 interacts with LIAS to mediate cuproptosis in cardiomyocytes during ischemia/reperfusion injury
PMID: 39930254
5
LIAS dysregulation contributes to neuronal cuproptosis and cognitive impairment induced by polystyrene nanoplastics
PMID: 40394693
Disease Associationsβ“˜21
lipoic acid synthetase deficiencyOpen Targets
0.80Strong
genetic disorderOpen Targets
0.41Moderate
neurodegenerative diseaseOpen Targets
0.34Weak
mitochondrial diseaseOpen Targets
0.19Weak
hemorrhoidOpen Targets
0.15Weak
breast cancerOpen Targets
0.08Suggestive
placenta praeviaOpen Targets
0.06Suggestive
esophageal squamous cell carcinomaOpen Targets
0.05Suggestive
cystic fibrosisOpen Targets
0.04Suggestive
cancerOpen Targets
0.04Suggestive
anencephaly 1Open Targets
0.03Suggestive
Isolated anencephaly/exencephalyOpen Targets
0.03Suggestive
atopic eczemaOpen Targets
0.03Suggestive
diabetic nephropathyOpen Targets
0.03Suggestive
gastric cancerOpen Targets
0.03Suggestive
infectionOpen Targets
0.03Suggestive
dental cariesOpen Targets
0.02Suggestive
SepsisOpen Targets
0.02Suggestive
neoplasmOpen Targets
0.02Suggestive
ulcerative colitisOpen Targets
0.02Suggestive
Hyperglycinemia, lactic acidosis, and seizuresUniProt
Pathogenic Variants32
NM_006859.4(LIAS):c.266dup (p.Asn89fs)Pathogenic
Lipoic acid synthetase deficiency
β˜…β˜…β˜†β˜†2026β†’ Residue 89
NM_006859.4(LIAS):c.954+1G>ALikely pathogenic
not provided|Lipoic acid synthetase deficiency
β˜…β˜…β˜†β˜†2025
NM_006859.4(LIAS):c.107dup (p.Glu37fs)Pathogenic
Lipoic acid synthetase deficiency|not provided
β˜…β˜…β˜†β˜†2025β†’ Residue 37
NM_006859.4(LIAS):c.649C>T (p.Arg217Ter)Pathogenic
Lipoic acid synthetase deficiency|not provided
β˜…β˜…β˜†β˜†2025β†’ Residue 217
NM_006859.4(LIAS):c.218+1G>ALikely pathogenic
Lipoic acid synthetase deficiency
β˜…β˜…β˜†β˜†2024
NM_006859.4(LIAS):c.100A>T (p.Lys34Ter)Pathogenic
Lipoic acid synthetase deficiency|not provided
β˜…β˜…β˜†β˜†2023β†’ Residue 34
NM_006859.4(LIAS):c.440dup (p.Thr148fs)Pathogenic
Lipoic acid synthetase deficiency
β˜…β˜…β˜†β˜†2023β†’ Residue 148
NM_006859.4(LIAS):c.277del (p.Lys92_Leu93insTer)Pathogenic
not provided|Lipoic acid synthetase deficiency
β˜…β˜…β˜†β˜†2023β†’ Residue 92
NM_006859.4(LIAS):c.236G>A (p.Trp79Ter)Likely pathogenic
Lipoic acid synthetase deficiency
β˜…β˜†β˜†β˜†2025β†’ Residue 79
NM_006859.4(LIAS):c.109G>T (p.Glu37Ter)Pathogenic
Lipoic acid synthetase deficiency
β˜…β˜†β˜†β˜†2025β†’ Residue 37
NM_006859.4(LIAS):c.328C>T (p.Arg110Ter)Pathogenic
Lipoic acid synthetase deficiency
β˜…β˜†β˜†β˜†2025β†’ Residue 110
NM_006859.4(LIAS):c.212del (p.Gly71fs)Pathogenic
Lipoic acid synthetase deficiency
β˜…β˜†β˜†β˜†2024β†’ Residue 71
NM_006859.4(LIAS):c.480del (p.Tyr161fs)Pathogenic
Lipoic acid synthetase deficiency
β˜…β˜†β˜†β˜†2024β†’ Residue 161
NM_006859.4(LIAS):c.692T>G (p.Leu231Ter)Pathogenic
Inborn genetic diseases
β˜…β˜†β˜†β˜†2024β†’ Residue 231
NM_006859.4(LIAS):c.367_389dup (p.Leu132fs)Pathogenic
Lipoic acid synthetase deficiency
β˜…β˜†β˜†β˜†2023β†’ Residue 132
NM_006859.4(LIAS):c.280A>T (p.Lys94Ter)Pathogenic
Lipoic acid synthetase deficiency
β˜…β˜†β˜†β˜†2023β†’ Residue 94
NM_006859.4(LIAS):c.520del (p.Tyr174fs)Pathogenic
Lipoic acid synthetase deficiency
β˜…β˜†β˜†β˜†2022β†’ Residue 174
NM_006859.4(LIAS):c.737+1G>ALikely pathogenic
Lipoic acid synthetase deficiency
β˜…β˜†β˜†β˜†2022
NM_006859.4(LIAS):c.130del (p.Asp44fs)Pathogenic
Lipoic acid synthetase deficiency
β˜…β˜†β˜†β˜†2022β†’ Residue 44
NM_006859.4(LIAS):c.884-1G>ALikely pathogenic
Lipoic acid synthetase deficiency
β˜…β˜†β˜†β˜†2022
View on ClinVar β†—
Related Genes
GCSHProtein interaction100%ANKRD54Protein interaction94%ISCUProtein interaction93%GLRX5Protein interaction91%BOLA1Protein interaction85%LYRM4Protein interaction84%
Tissue Expression6 tissues
Heart
100%
Liver
78%
Ovary
57%
Brain
46%
Bone Marrow
37%
Lung
28%
Gene Interaction Network
Click a node to explore
LIASGCSHANKRD54ISCUGLRX5BOLA1LYRM4
PROTEIN STRUCTURE
Preparing viewer…
PDB8TRW Β· 1.54 Γ… Β· X-ray
View on RCSB β†—
Constraintβ“˜
LOEUFβ“˜
0.99LoF Tolerant
pLIβ“˜
0.00Tolerant
Observed/Expected LoF0.72 [0.53–0.99]
RankingsWhere LIAS stands among ~20K protein-coding genes
  • #12,817of 20,598
    Most Researched26
  • #1,767of 5,498
    Most Pathogenic Variants32
  • #9,476of 17,882
    Most Constrained (LOEUF)0.99
Genes detectedLIAS
Sources retrieved10 papers
Response timeβ€”
πŸ“„ Sources
10β–Ό
1
A cuproptosis nanocapsule for cancer radiotherapy.
PMID: 39300223
Nat Nanotechnol Β· 2024
1.00
2
Triptolide-induced cuproptosis is a novel antitumor strategy for the treatment of cervical cancer.
PMID: 39198750
Cell Mol Biol Lett Β· 2024
0.90
3
FDX1 regulates cellular protein lipoylation through direct binding to LIAS.
PMID: 37453661
J Biol Chem Β· 2023
0.80
4
Copper's dual role: unravelling the link between copper homeostasis, cuproptosis, and cardiovascular diseases.
PMID: 38467792
Hypertens Res Β· 2024
0.70
5
Identification of hub cuproptosis related genes and immune cell infiltration characteristics in periodontitis.
PMID: 37215133
Front Immunol Β· 2023
0.60